Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

Journal article

Tau is a microtubule binding protein implicated in a number of human neurodegenerative disorders, including Alzheimer's disease. Phosphorylation of serine-proline/threonine-proline sites, targeted by proline-directed kinases, coincides temporally with neurodegeneration in the human diseases. Recently, we demonstrated that this unique group of serines and threonines has a critical role in controlling tau toxicity in a Drosophila model of tauopathy. Here, we use a combination of genetic and bio...

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Authors: Steinhilb, M; Dias-Santagata, D; Fulga, T; Felch, D; Feany, M

• Journal: Molecular biology of the cell
• Volume: 18
• Issue: 12
• Pages: 5060-5068
• Publication date: 2007-12-01
• DOI: 10.1091/mbc.e07-04-0327
• EISSN: 1939-4586
• ISSN: 1059-1524
• Language: English
• Keywords: Phosphorylation; Electrophoresis, Polyacrylamide Gel; Animals; tau Proteins; Signal Transduction; Amino Acids; Protein Kinases; Phosphatidylinositol 3-Kinases; Cell Cycle; Drosophila Proteins; Animals, Genetically Modified; Neurons; Mutation; Drosophila melanogaster